8ZC5

SARS-CoV-2 Omicron BA.4 spike trimer (6P) in complex with D1F6 Fab, focused refinement of RBD region

Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.91 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history. 


Literature

An unconventional VH1-2 antibody tolerates escape mutations and shows an antigenic hotspot on SARS-CoV-2 spike

Liu, B., Niu, X., Deng, Y., Zhang, Z., Wang, Y., Gao, X., Liang, H., Li, Z., Wang, Q., Cheng, Y., Chen, Q., Huang, S., Pan, Y., Su, M., Lin, X., Niu, C., Chen, Y., Yang, W., Zhang, Y., Yan, Q., He, J., Zhao, J., Chen, L., Xiong, X.

To be published.

Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Spike protein S1
A, B
196Severe acute respiratory syndrome coronavirus 2Mutation(s): 17 
Gene Names: S, 2
UniProt
Find proteins for P0DTC2 (Severe acute respiratory syndrome coronavirus 2)
Explore P0DTC2 
Go to UniProtKB:  P0DTC2
Entity Groups  
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UniProt GroupP0DTC2
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Light chain of D1F6 Fab
C, D
110Homo sapiensMutation(s): 0 
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Sequence Annotations
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Heavy chain of D1F6 Fab
E, F
127Homo sapiensMutation(s): 0 
Entity Groups  
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Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.91 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

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View more in-depth experimental data
Entry History & Funding Information

Deposition Data

Funding OrganizationLocationGrant Number
Other governmentEKPG21-06
Other governmentSRPG22-002
Other government2021A1515011289

Revision History  (Full details and data files)

  • Version 1.0: 2024-05-15
    Type: Initial release